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| Description | The N-terminal segment (residues 34–45) of human α-synuclein (the major Lewy-body component), involved in membrane binding and aggregation; used for misfolding, aggregation and Parkinson's immune-epitope studies. |
Product Basic Information Table
| Product Standard English Name | Product Abbreviation / Alias | Function Tags (comma-separated) | Core Structure | Molecular Formula | Exact Mass (Da) | Average MW (Da) | Salt Form | Length (aa) |
| alpha-Synuclein (34-45) (human) | Human alpha-synuclein (34-45) fragment, KEGVLYVGSKTK, SNCA 34-45, N-terminal amphipathic repeat fragment, CAS 2170181-52-7 | Alpha-synuclein, Parkinson's disease, Synucleinopathies, Amyloid aggregation, N-terminal amphipathic repeat | KEGVLYVGSKTK (H-Lys-Glu-Gly-Val-Leu-Tyr-Val-Gly-Ser-Lys-Thr-Lys-OH, linear 12-mer, human SNCA residues 34-45) | C59H101N15O18 | 1307.74 | 1308.54 | Free peptide (neutral per published formula; Bachem CAS 2170181-52-7 also offers a TFA salt form) | 12 |
Physicochemical Solubility & Storage Parameters
| Product Code | Appearance | Long-term Storage | Short-term Storage | Solution Stability | Solid Powder Stability |
| PEP-ASYN-01 | powder, white to off-white (Bachem etc., purity >=95% HPLC; CAS 2170181-52-7) | Store frozen below -20 C, dry, tightly sealed and protected from light (stable approx. 2-3 years as powder) | Short-term at 4 C sealed and dry; after reconstitution, aliquot and store at -20 C or -80 C; avoid repeated freeze-thaw | Net charge +2 (3 Lys, 1 Glu), reasonably hydrophilic, soluble in sterile water or acidic buffer; however alpha-synuclein fragments have aggregation propensity and contain the central hydrophobic Leu-Tyr-Val motif. Use immediately after reconstitution or aliquot and freeze; if needed, pre-dissolve with a small amount of DMSO and sonicate. Avoid repeated freeze-thaw and prolonged room-temperature storage | powder stable long-term (approx. 2-3 years) at -20 C, dry, sealed and light-protected; keep moisture-proof. alpha-Synuclein peptides have intrinsic aggregation/amyloidogenic propensity; the solid state is relatively stable, weigh promptly after opening and reseal |
Functional Description
| Product Code | Frontend Short Summary | Detailed Biological Function Description | Applicable Research Areas (comma-separated) | Targets / Pathways |
| PEP-ASYN-01 | Human alpha-synuclein residues 34-45 (KEGVLYVGSKTK), located in the N-terminal KTKEGV amphipathic repeat region, for studies of protein aggregation and membrane binding in Parkinson's disease and synucleinopathies. | This is the human alpha-synuclein (SNCA, 140 aa) fragment residues 34-45, KEGVLYVGSKTK (CAS 2170181-52-7). It lies in the N-terminal Lys-rich 11-mer repeat region (KTKEGV motif), is positively charged and amphipathic, and exists as an intrinsically disordered state in solution, adopting an amphipathic alpha-helix upon membrane binding. Misfolding and aggregation of alpha-synuclein into Lewy bodies is the hallmark of Parkinson's disease (PD) and synucleinopathies such as multiple system atrophy. The 34-45 fragment is used to study N-terminal-repeat membrane binding, amphipathic helical conformation and peptide aggregation/amyloid nucleation. Supplied as the published neutral peptide C59H101N15O18 (avg MW 1308.5); suppliers also commonly offer a TFA salt form. | Parkinson's disease, Synucleinopathies, Protein misfolding and aggregation, Neurodegeneration, Amyloid | alpha-Synuclein (SNCA) N-terminal repeats; Phospholipid membrane binding |
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